| 纯度 | >90%SDS-PAGE. |
| 种属 | Human |
| 靶点 | pbpC |
| Uniprot No | P76577 |
| 内毒素 | < 0.01EU/μg |
| 表达宿主 | E.coli |
| 表达区间 | 1-770aa |
| 氨基酸序列 | MPRLLTKRGCWITLAAAPFLLFLAAWGADKLWPLPLHEVNPARVVVAQDGTPLWRFADADGIWRYPVTIEDVSPRYLEALINYEDRWFWKHPGVNPFSVARAAWQDLTSGRVISGGSTLTMQVARLLDPHPKTFGGKIRQLWRALQLEWHLSKREILTLYLNRAPFGGTLQGIGAASWAYLGKSPANLSYSEAAMLAVLPQAPSRLRPDRWPERAEAARNKVLERMAVQGVWSREQVKESREEPIWLAPRQMPQLAPLFSRMMLGKSKSDKITTTLDAGLQRRLEELAQNWKGRLPPRSSLAMIVVDHTDMRVRGWVGSVDLNDDSRFGHVDMVNSIRSPGSVLKPFVYGLALDEGLIHPASLLQDVPRRTGDYRPGNFDSGFHGPISMSEALVRSLNLPAVQVLEAYGPKRFAAKLRNVGLPLYLPNGAAPNLSLILGGAGAKLEDMAAAYTAFARHGKAGKLRLQPDDPLLERPLMSSGAAWIIRRIMADEAQPLPDSALPRVAPLAWKTGTSYGYRDAWAIGVNARYVIGIWTGRPDGTPVVGQFGFASAVPLLNQVNNILLSRSANLPEDPRPNSVTRGVICWPGGQSLPEGDGNCRRRLATWLLDGSQPPTLLLPEQEGINGIRFPIWLDENGKRVAADCPQARQEMINVWPLPLEPWLPASERRAVRLPPASTSCPPYGHDAQLPLQLTGVRDGAIIKRLPGAAEATLPLQSSGGAGERWWFLNGEPLTERGRNVTLHLTDKGDYQLLVMDDVGQIATVKFVMQ |
| 预测分子量 | 85 kDa |
| 蛋白标签 | His tag N-Terminus |
| 缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
| 稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
| 复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是3篇与pbpC重组蛋白相关的模拟参考文献(内容基于领域常见研究方向整合，请使用时核实原文)：
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1. **标题**: *Cloning and Expression of the pbpC Gene Encoding Penicillin-Binding Protein 3 in Escherichia coli*
**作者**: Müller, H., et al.
**摘要**: 研究报道了从肺炎链球菌中克隆pbpC基因，并利用大肠杆菌表达系统实现重组蛋白的高效表达。通过质谱和Western blot验证蛋白纯度，为后续研究其与β-内酰胺类抗生素的相互作用提供基础。
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2. **标题**: *Structural Analysis of Recombinant PBPc in Methicillin-Resistant Staphylococcus aureus*
**作者**: Tanaka, K., & Watanabe, T.
**摘要**: 通过X射线晶体学解析了重组PBPc的三维结构，揭示了其与青霉素结合的活性位点突变特征，阐明了该蛋白在金黄色葡萄球菌甲氧西林耐药性中的分子机制。
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3. **标题**: *Functional Characterization of Recombinant pbpC in Streptococcus pneumoniae β-Lactam Resistance*
**作者**: García, E., et al.
**摘要**: 利用基因敲除和重组蛋白回补实验，证明pbpC编码的青霉素结合蛋白可通过改变肽聚糖交联模式降低肺炎链球菌对头孢类抗生素的敏感性，为耐药性进化研究提供依据。
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**注意**：以上文献信息为模拟生成，实际引用请通过PubMed/Google Scholar检索关键词(如“pbpC recombinant protein”“penicillin-binding protein expression”)获取真实文献。
**Background of PBP2x (pbpC) Recombinant Protein**
Penicillin-binding protein 2x (PBP2x), encoded by the *pbpC* gene in some bacterial species, is a critical enzyme involved in peptidoglycan biosynthesis, a process essential for bacterial cell wall integrity and growth. As a member of the penicillin-binding protein (PBP) family, PBP2x exhibits transpeptidase and transglycosylase activities, facilitating the cross-linking of peptidoglycan strands during cell wall assembly. Its function makes it a primary target for β-lactam antibiotics (e.g., penicillins, cephalosporins), which inhibit PBPs by mimicking their substrate and disrupting cell wall synthesis.
In pathogenic bacteria, such as *Streptococcus pneumoniae*, mutations in *pbpC* are closely associated with β-lactam resistance. Altered PBP2x variants with reduced antibiotic affinity enable bacterial survival under therapeutic pressure, contributing to the global challenge of antimicrobial resistance (AMR). Studying PBP2x’s structure-function relationships and resistance mechanisms is thus vital for developing novel antibiotics or inhibitors.
Recombinant PBP2x production involves cloning the *pbpC* gene into expression vectors (e.g., *E. coli* or yeast systems) to produce purified, functional protein for biochemical and structural analyses. This approach allows researchers to characterize enzymatic activity, screen for inhibitors, and resolve high-resolution structures (via X-ray crystallography or cryo-EM), revealing drug-binding sites and resistance-conferring mutations.
Beyond drug discovery, recombinant PBP2x serves as an antigen for diagnostic assays or vaccine development against resistant strains. Its study also advances synthetic biology, enabling engineering of cell wall-modifying enzymes for biotechnological applications. Overall, PBP2x recombinant protein research bridges microbiology, structural biology, and medicine, addressing both fundamental science and clinical needs in the AMR era.
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